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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...

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Related Experiment Video

Updated: May 21, 2026

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
05:58

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells

Published on: February 24, 2026

Lysine post-translational modifications and the cytoskeleton.

Wendy D Zencheck1, Hui Xiao, Louis M Weiss

  • 1Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, U.S.A.

Essays in Biochemistry
|June 20, 2012
PubMed
Summary

Post-translational modifications (PTMs) of lysine residues regulate gene expression and protein interactions. This chapter explores how lysine PTMs, including acetylation, ubiquitination, and SUMOylation, control the eukaryotic cytoskeleton.

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Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
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Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Related Experiment Videos

Last Updated: May 21, 2026

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
05:58

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells

Published on: February 24, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Post-translational modifications (PTMs) of lysine residues are crucial for regulating gene expression, protein interactions, and degradation.
  • The cytoskeleton, essential for cell motility, structure, and intracellular transport, relies on complex protein assemblies for regulation.
  • Lysine PTMs play a significant role in modulating the function of cytoskeletal components.

Purpose of the Study:

  • To investigate the role of lysine post-translational modifications in regulating the eukaryotic cytoskeleton.
  • To focus on acetylation, ubiquitination, and SUMOylation of cytoskeletal proteins.
  • To discuss the biological importance of these modifications for cytoskeletal function.

Main Methods:

  • Review of existing literature on lysine PTMs and cytoskeletal regulation.
  • Focus on acetylation, ubiquitination, and SUMOylation.
  • Analysis of PTMs in microfilaments, intermediate filaments, and microtubules.

Main Results:

  • Lysine acetylation is identified as a key regulator affecting all three major classes of cytoskeletal filaments.
  • Ubiquitination and SUMOylation also play important roles in the regulation and processing of cytoskeletal proteins.
  • PTMs on lysine residues are critical for the dynamic assembly and function of the cytoskeleton.

Conclusions:

  • Lysine PTMs are fundamental regulators of cytoskeletal organization and dynamics.
  • Acetylation, ubiquitination, and SUMOylation are key PTMs impacting cytoskeletal proteins.
  • Understanding these modifications provides insights into cellular processes like motility, transport, and division.